UBX2B_MOUSE - dbPTM
UBX2B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBX2B_MOUSE
UniProt AC Q0KL01
Protein Name UBX domain-containing protein 2B
Gene Name Ubxn2b
Organism Mus musculus (Mouse).
Sequence Length 331
Subcellular Localization Nucleus . Cytoplasm, cytosol . Endoplasmic reticulum . Golgi apparatus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Localizes to centrosome during mitotic prophase and metaphase.
Protein Description Adapter protein required for Golgi and endoplasmic reticulum biogenesis. Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis. The complex formed with VCP has membrane fusion activity; membrane fusion activity requires USO1-GOLGA2 tethering and BET1L. VCPIP1 is also required, but not its deubiquitinating activity. Together with NSFL1C/p47, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase. Also, regulates spindle orientation during mitosis..
Protein Sequence MAEGGRAEPEEQERGSSRPRPPSARDLQLALAELYEDEMKCKSSKPDRSTPATCRSPRTPPHRLYSGDHKYDGLHIVQPPTGKIVNELFKEAREHGAVPLNEATRSSREDKTKSFTGGGYRLGNSFYKRSEYIYGENQLQDVQVLLKLWRNGFSLDDGELRPYSDPTNAQFLESVKRGETPLELQRLVHGAQVNLDMEDHQDQEYIKPRLRFKAFSGEGQKLGSLTPEIVSTPSSPEEEDKSILNAAVLIDDSMPTTKIQIRLADGSRLVQRFNSTHRILDVRDFIVRSRPEFATTDFILVTSFPSKELTDETVTLQEADILNTVILQQLK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAEGGRAEP
------CCCCCCCCH
24.92-
23PhosphorylationSSRPRPPSARDLQLA
CCCCCCCCHHHHHHH
38.3229472430
50PhosphorylationSSKPDRSTPATCRSP
CCCCCCCCCCCCCCC
20.17-
53PhosphorylationPDRSTPATCRSPRTP
CCCCCCCCCCCCCCC
15.0629514104
56PhosphorylationSTPATCRSPRTPPHR
CCCCCCCCCCCCCCC
22.3829472430
59PhosphorylationATCRSPRTPPHRLYS
CCCCCCCCCCCCCCC
44.5522817900
66PhosphorylationTPPHRLYSGDHKYDG
CCCCCCCCCCCCCCC
42.1922817900
107PhosphorylationLNEATRSSREDKTKS
CCHHHCCCCCCCCCC
36.0829899451
154PhosphorylationKLWRNGFSLDDGELR
HHHHCCCCCCCCCCC
32.0829899451
216PhosphorylationRLRFKAFSGEGQKLG
EEEEEEECCCCCCCC
40.5725521595
224PhosphorylationGEGQKLGSLTPEIVS
CCCCCCCCCCCCHHC
39.2325619855
226PhosphorylationGQKLGSLTPEIVSTP
CCCCCCCCCCHHCCC
22.1425619855
231PhosphorylationSLTPEIVSTPSSPEE
CCCCCHHCCCCCHHH
40.0225619855
232PhosphorylationLTPEIVSTPSSPEEE
CCCCHHCCCCCHHHH
19.1225619855
234PhosphorylationPEIVSTPSSPEEEDK
CCHHCCCCCHHHHHH
59.6225521595
235PhosphorylationEIVSTPSSPEEEDKS
CHHCCCCCHHHHHHH
37.2225521595
242PhosphorylationSPEEEDKSILNAAVL
CHHHHHHHHHHHHHC
44.6323649490

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of UBX2B_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBX2B_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UBX2B_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UBX2B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBX2B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND MASSSPECTROMETRY.

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